1. GLYCOPROTEINS Dr Amina Tariq Biochemistry

2. Glycoproteins Glycoproteins are proteins that contain oligosaccharide (glycan) chains covalently attached to their polypeptide backbones.

3. Almost all the plasma proteins of humans—except albumin—are glycoproteins. Many proteins of cellular membranes contain substantial amounts of carbohydrate.

4. A number of the blood group substances are glycoproteins. Certain hormones (eg, chorionic gonadotropin) are glycoproteins.

5. They differ from proteoglycans: 1. Length of the chain is relatively short (usually 2-10 sugar residues) very long in GAGs. 2. Do not have repeating disaccharide units. 3. They are branched. 4. May or may not be negatively charged.

6. Glycoproteins occur in most organisms, from bacteria to humans. Their carbohydrate content ranges from 1% to over 85% by weight. They perform the following functions:

7. FunctionExample Structural roleCollagen Transport roleTransferrin Immunologic roleImmunoglobulins Cell-to-cell communication Selectins Proteins in fertilization Cell adhesion molecules Cell signallingMany receptors ClottingPlasma proteins Lipoproteins LubricationMucins

8. Hormones HCG, TSH Anti freeze cold water fish

9. Some of the processes involving glycoproteins:  inflammation  blood clotting  peptic ulcers  AIDS (HIV)

10.  influenza  fertilization  cancer  cystic fibrosis  arthritis

13. The predominant sugars found in glycoproteins are: glucose (Glc), galactose (Gal), mannose (Man), fucose (Fuc),

14. N-acetylgalactosamine (GalNAc), N-acetylglucosamine (GlcNAc) and N-acetylneuraminic acid (NANA). NANA is also called sialic acid.

15. The distinction between proteoglycans and glycoproteins resides in the level and types of carbohydrate modification.

16. Proteoglycans also contain the sugar glucuronic acid (GlcA). The carbohydrate modifications found in glycoproteins are rarely as complex as that of proteoglycans.

17. The carbohydrates of glycoproteins are linked to the protein component through either O-glycosidic or N-glycosidic bonds.

18. The N-glycosidic linkage is through the amide group of asparagine (Asn, N). The O-glycosidic linkage is to the hydroxyl of serine (Ser, S), threonine (Thr, T) or hydroxylysine (hLys).

19. O-linked sugars: May be membrane glycoprotein components Or extracellular glycoproteins.

20. When attached to Ser or Thr, the sugar of O-linked glycoproteins is most often GalNAc.

21. N-linked sugars: The predominant carbohydrate attachment in glycoproteins of mammalian cells is via N-glycosidic linkage.

22. They are of two types: 1. Complex oligosaccharides 2. High mannose oligosaccharides

23. Their core pentasaccharide is the same. In the complex form additional sugar residues are present: N-acetylglucosamine (GlcNAc) and N-acetylneuraminic acid (NANA). Fucose

24. High mannose contain only mannose residues

25. Most proteins that are secreted, or bound to the plasma membrane, are modified by carbohydrate attachment. The part that is modified, in plasma membrane-bound proteins, is the extracellular portion of the protein.

26. Intracellular proteins are less frequently modified by carbohydrate attachment. However, the attachment of carbohydrate to intracellular proteins confers unique functional activities on these proteins

27. I – cell disease Cancers Metastasis